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PDBsum entry 2ojg

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Transferase PDB id
2ojg
Jmol
Contents
Protein chain
337 a.a.
Ligands
SO4
19A
Waters ×188
HEADER    TRANSFERASE                             12-JAN-07   2OJG
TITLE     CRYSTAL STRUCTURE OF ERK2 IN COMPLEX WITH N,N-DIMETHYL-4-(4-
TITLE    2 PHENYL-1H-PYRAZOL-3-YL)-1H-PYRROLE-2-CARBOXAMIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: EXTRACELLULAR SIGNAL-REGULATED KINASE 2, ERK-2,
COMPND   5 MITOGEN-ACTIVATED PROTEIN KINASE 2, MAP KINASE 2, MAPK 2,
COMPND   6 P42-MAPK, ERT1;
COMPND   7 EC: 2.7.11.24;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: MAPK1, ERK2, PRKM1;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PT7BLUE
KEYWDS    KINASE INHIBITOR, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    X.XIE,M.D.JACOBS
REVDAT   3   24-FEB-09 2OJG    1       VERSN
REVDAT   2   27-MAR-07 2OJG    1       JRNL
REVDAT   1   06-FEB-07 2OJG    0
JRNL        AUTH   A.M.ARONOV,C.BAKER,G.W.BEMIS,J.CAO,G.CHEN,P.J.FORD,
JRNL        AUTH 2 U.A.GERMANN,J.GREEN,M.R.HALE,M.JACOBS,J.W.JANETKA,
JRNL        AUTH 3 F.MALTAIS,G.MARTINEZ-BOTELLA,M.N.NAMCHUK,J.STRAUB,
JRNL        AUTH 4 Q.TANG,X.XIE
JRNL        TITL   FLIPPED OUT: STRUCTURE-GUIDED DESIGN OF SELECTIVE
JRNL        TITL 2 PYRAZOLYLPYRROLE ERK INHIBITORS.
JRNL        REF    J.MED.CHEM.                   V.  50  1280 2007
JRNL        REFN                   ISSN 0022-2623
JRNL        PMID   17300186
JRNL        DOI    10.1021/JM061381F
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNX 2005
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK   3               : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK   3               : YIP,DZAKULA)
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.97
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 766664.688
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.9
REMARK   3   NUMBER OF REFLECTIONS             : 23756
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220
REMARK   3   R VALUE            (WORKING SET) : 0.216
REMARK   3   FREE R VALUE                     : 0.260
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 2164
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : 0.2330
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : 0.2290
REMARK   3   FREE R VALUE                    (NO CUTOFF) : 0.272
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : 9.100
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : 2164
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 23756
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 72.90
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2841
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2440
REMARK   3   BIN FREE R VALUE                    : 0.3030
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.50
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 299
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2756
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 26
REMARK   3   SOLVENT ATOMS            : 188
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 22.10
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.40
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -5.73000
REMARK   3    B22 (A**2) : 2.60000
REMARK   3    B33 (A**2) : 3.13000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -1.87000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.24
REMARK   3   ESD FROM SIGMAA              (A) : 0.14
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.30
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.17
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 1.20
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.60
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.59
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.360 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.080 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.080 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.020 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.35
REMARK   3   BSOL        : 50.40
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : INHIB.PAR
REMARK   3  PARAMETER FILE  4  : PARMXRAY.XPL
REMARK   3  PARAMETER FILE  5  : ION.PARAM
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2OJG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JAN-07.
REMARK 100 THE RCSB ID CODE IS RCSB041211.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-SEP-99
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.2
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23772
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.1
REMARK 200  DATA REDUNDANCY                : 2.770
REMARK 200  R MERGE                    (I) : 0.04800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 45.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 14 MG/ML, 20 MM TRIS, PH
REMARK 280  7.0, 5 MM DTT, 200 MM NACL. PRECIPITANT: 100 MM HEPES, PH 7.2,
REMARK 280  28-30% PEG-MME-2000, 200 MM AMMONIUM SULFATE, 20 MM 2-ME,
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       35.38800
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A   -21
REMARK 465     GLY A   -20
REMARK 465     SER A   -19
REMARK 465     SER A   -18
REMARK 465     HIS A   -17
REMARK 465     HIS A   -16
REMARK 465     HIS A   -15
REMARK 465     HIS A   -14
REMARK 465     HIS A   -13
REMARK 465     HIS A   -12
REMARK 465     SER A   -11
REMARK 465     SER A   -10
REMARK 465     GLY A    -9
REMARK 465     LEU A    -8
REMARK 465     VAL A    -7
REMARK 465     PRO A    -6
REMARK 465     ARG A    -5
REMARK 465     GLY A    -4
REMARK 465     SER A    -3
REMARK 465     HIS A    -2
REMARK 465     MET A    -1
REMARK 465     ALA A     0
REMARK 465     ALA A     1
REMARK 465     ALA A     2
REMARK 465     ALA A     3
REMARK 465     ALA A     4
REMARK 465     ALA A     5
REMARK 465     GLY A     6
REMARK 465     ALA A     7
REMARK 465     GLY A     8
REMARK 465     PRO A     9
REMARK 465     GLU A    10
REMARK 465     MET A    11
REMARK 465     VAL A    12
REMARK 465     ARG A    13
REMARK 465     GLY A    14
REMARK 465     GLN A    15
REMARK 465     VAL A    16
REMARK 465     ASP A   330
REMARK 465     MET A   331
REMARK 465     TYR A   356
REMARK 465     ARG A   357
REMARK 465     SER A   358
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASN A  25       38.98     70.15
REMARK 500    LYS A  46       -5.27     61.23
REMARK 500    SER A  55       74.65   -118.64
REMARK 500    PHE A  57       24.82    -71.48
REMARK 500    ARG A 146       -2.74     79.84
REMARK 500    ASP A 147       42.34   -142.72
REMARK 500    ASP A 165       86.16     64.17
REMARK 500    ASN A 199       16.08   -160.73
REMARK 500    LEU A 292       49.05    -99.10
REMARK 500    ASP A 316       89.18   -159.64
REMARK 500    ASP A 335       51.88   -116.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 PHE A  327     LYS A  328                 -131.15
REMARK 500 LYS A  328     PHE A  329                  115.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 516        DISTANCE =  6.22 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 359
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19A A 360
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2OJI   RELATED DB: PDB
REMARK 900 RELATED ID: 2OJJ   RELATED DB: PDB
REMARK 900 RELATED ID: 2OK1   RELATED DB: PDB
DBREF  2OJG A    0   358  UNP    P28482   MK01_HUMAN       1    359
SEQADV 2OJG MET A  -21  UNP  P28482              CLONING ARTIFACT
SEQADV 2OJG GLY A  -20  UNP  P28482              CLONING ARTIFACT
SEQADV 2OJG SER A  -19  UNP  P28482              CLONING ARTIFACT
SEQADV 2OJG SER A  -18  UNP  P28482              CLONING ARTIFACT
SEQADV 2OJG HIS A  -17  UNP  P28482              EXPRESSION TAG
SEQADV 2OJG HIS A  -16  UNP  P28482              EXPRESSION TAG
SEQADV 2OJG HIS A  -15  UNP  P28482              EXPRESSION TAG
SEQADV 2OJG HIS A  -14  UNP  P28482              EXPRESSION TAG
SEQADV 2OJG HIS A  -13  UNP  P28482              EXPRESSION TAG
SEQADV 2OJG HIS A  -12  UNP  P28482              EXPRESSION TAG
SEQADV 2OJG SER A  -11  UNP  P28482              CLONING ARTIFACT
SEQADV 2OJG SER A  -10  UNP  P28482              CLONING ARTIFACT
SEQADV 2OJG GLY A   -9  UNP  P28482              CLONING ARTIFACT
SEQADV 2OJG LEU A   -8  UNP  P28482              CLONING ARTIFACT
SEQADV 2OJG VAL A   -7  UNP  P28482              CLONING ARTIFACT
SEQADV 2OJG PRO A   -6  UNP  P28482              CLONING ARTIFACT
SEQADV 2OJG ARG A   -5  UNP  P28482              CLONING ARTIFACT
SEQADV 2OJG GLY A   -4  UNP  P28482              CLONING ARTIFACT
SEQADV 2OJG SER A   -3  UNP  P28482              CLONING ARTIFACT
SEQADV 2OJG HIS A   -2  UNP  P28482              CLONING ARTIFACT
SEQADV 2OJG MET A   -1  UNP  P28482              CLONING ARTIFACT
SEQRES   1 A  380  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 A  380  LEU VAL PRO ARG GLY SER HIS MET ALA ALA ALA ALA ALA
SEQRES   3 A  380  ALA GLY ALA GLY PRO GLU MET VAL ARG GLY GLN VAL PHE
SEQRES   4 A  380  ASP VAL GLY PRO ARG TYR THR ASN LEU SER TYR ILE GLY
SEQRES   5 A  380  GLU GLY ALA TYR GLY MET VAL CYS SER ALA TYR ASP ASN
SEQRES   6 A  380  VAL ASN LYS VAL ARG VAL ALA ILE LYS LYS ILE SER PRO
SEQRES   7 A  380  PHE GLU HIS GLN THR TYR CYS GLN ARG THR LEU ARG GLU
SEQRES   8 A  380  ILE LYS ILE LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE
SEQRES   9 A  380  GLY ILE ASN ASP ILE ILE ARG ALA PRO THR ILE GLU GLN
SEQRES  10 A  380  MET LYS ASP VAL TYR ILE VAL GLN ASP LEU MET GLU THR
SEQRES  11 A  380  ASP LEU TYR LYS LEU LEU LYS THR GLN HIS LEU SER ASN
SEQRES  12 A  380  ASP HIS ILE CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY
SEQRES  13 A  380  LEU LYS TYR ILE HIS SER ALA ASN VAL LEU HIS ARG ASP
SEQRES  14 A  380  LEU LYS PRO SER ASN LEU LEU LEU ASN THR THR CYS ASP
SEQRES  15 A  380  LEU LYS ILE CYS ASP PHE GLY LEU ALA ARG VAL ALA ASP
SEQRES  16 A  380  PRO ASP HIS ASP HIS THR GLY PHE LEU THR GLU TYR VAL
SEQRES  17 A  380  ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET LEU ASN
SEQRES  18 A  380  SER LYS GLY TYR THR LYS SER ILE ASP ILE TRP SER VAL
SEQRES  19 A  380  GLY CYS ILE LEU ALA GLU MET LEU SER ASN ARG PRO ILE
SEQRES  20 A  380  PHE PRO GLY LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE
SEQRES  21 A  380  LEU GLY ILE LEU GLY SER PRO SER GLN GLU ASP LEU ASN
SEQRES  22 A  380  CYS ILE ILE ASN LEU LYS ALA ARG ASN TYR LEU LEU SER
SEQRES  23 A  380  LEU PRO HIS LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE
SEQRES  24 A  380  PRO ASN ALA ASP SER LYS ALA LEU ASP LEU LEU ASP LYS
SEQRES  25 A  380  MET LEU THR PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU
SEQRES  26 A  380  GLN ALA LEU ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP
SEQRES  27 A  380  PRO SER ASP GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE
SEQRES  28 A  380  ASP MET GLU LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS
SEQRES  29 A  380  GLU LEU ILE PHE GLU GLU THR ALA ARG PHE GLN PRO GLY
SEQRES  30 A  380  TYR ARG SER
HET    SO4  A 359       5
HET    19A  A 360      21
HETNAM     SO4 SULFATE ION
HETNAM     19A N,N-DIMETHYL-4-(4-PHENYL-1H-PYRAZOL-3-YL)-1H-PYRROLE-
HETNAM   2 19A  2-CARBOXAMIDE
FORMUL   2  SO4    O4 S 2-
FORMUL   3  19A    C16 H16 N4 O
FORMUL   4  HOH   *188(H2 O)
HELIX    1   1 HIS A   59  PHE A   76  1                                  18
HELIX    2   2 LEU A  110  GLN A  117  1                                   8
HELIX    3   3 SER A  120  ALA A  141  1                                  22
HELIX    4   4 LYS A  149  SER A  151  5                                   3
HELIX    5   5 ASP A  173  ASP A  177  5                                   5
HELIX    6   6 THR A  188  ARG A  192  5                                   5
HELIX    7   7 ALA A  193  MET A  197  5                                   5
HELIX    8   8 LYS A  205  ASN A  222  1                                  18
HELIX    9   9 HIS A  230  GLY A  243  1                                  14
HELIX   10  10 SER A  246  ILE A  253  1                                   8
HELIX   11  11 ASN A  255  SER A  264  1                                  10
HELIX   12  12 PRO A  272  PHE A  277  1                                   6
HELIX   13  13 ASP A  281  LEU A  292  1                                  12
HELIX   14  14 GLU A  301  ALA A  307  1                                   7
HELIX   15  15 HIS A  308  GLU A  312  5                                   5
HELIX   16  16 ASP A  316  GLU A  320  5                                   5
HELIX   17  17 GLU A  339  THR A  349  1                                  11
HELIX   18  18 ALA A  350  GLN A  353  5                                   4
SHEET    1   A 5 TYR A  23  GLY A  32  0
SHEET    2   A 5 GLY A  35  ASP A  42 -1  O  SER A  39   N  SER A  27
SHEET    3   A 5 ARG A  48  ILE A  54 -1  O  VAL A  49   N  ALA A  40
SHEET    4   A 5 VAL A  99  GLN A 103 -1  O  VAL A  99   N  ILE A  54
SHEET    5   A 5 ILE A  84  ILE A  88 -1  N  ASP A  86   O  VAL A 102
SHEET    1   B 3 THR A 108  ASP A 109  0
SHEET    2   B 3 LEU A 153  LEU A 155 -1  O  LEU A 155   N  THR A 108
SHEET    3   B 3 LEU A 161  ILE A 163 -1  O  LYS A 162   N  LEU A 154
SHEET    1   C 2 VAL A 143  LEU A 144  0
SHEET    2   C 2 ARG A 170  VAL A 171 -1  O  ARG A 170   N  LEU A 144
SITE     1 AC1  4 ARG A 189  ARG A 192  TYR A 231  HOH A 498
SITE     1 AC2 15 ILE A  29  TYR A  34  VAL A  37  ALA A  50
SITE     2 AC2 15 LYS A  52  ILE A  82  GLN A 103  ASP A 104
SITE     3 AC2 15 LEU A 105  MET A 106  ASP A 109  LYS A 112
SITE     4 AC2 15 LEU A 154  ASP A 165  HOH A 387
CRYST1   48.665   70.776   60.141  90.00 109.03  90.00 P 1 21 1      2
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.020549  0.000000  0.007088        0.00000
SCALE2      0.000000  0.014129  0.000000        0.00000
SCALE3      0.000000  0.000000  0.017589        0.00000
      
PROCHECK
Go to PROCHECK summary
 References